1IDS | Superoxide Dismutase | date | Sep 29, 1994 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
authors | J.B.Cooper, K.Mcintyre, S.P.Wood, Y.Zhang, D.Young | ||||||||||||||
compound | source | ||||||||||||||
Iron-Dependent Superoxide Dismutase (E.C.1.15.1.1) (Fe-Superoxide Dismutase, Fe-Sod) |
Mycobacterium Tuberculosis) Recombinant Form Expressed In (Mycobacterium Vaccae) | ||||||||||||||
symmetry | Space Group: P 21 | R_factor | 0.167 | ||||||||||||
crystal cell |
| ||||||||||||||
method | X-Ray Diffraction | resolution | 2.0 Å | ||||||||||||
ligand | FE | enzyme | Superoxide dismutase;. Superoxidase dismutase;. Copper-zinc superoxide dismutase;. Cu-Zn superoxide dismutase;. Ferrisuperoxide dismutase;. Superoxide dismutase I;. Superoxide dismutase II;. SOD;. Cu,Zn-SOD;. Mn-SOD;. Fe-SOD;. SODF;. SODS;. SOD-1;. SOD-2;. SOD-3;. SOD-4;. Hemocuprein;. Erythrocuprein;. Cytocuprein;. Cuprein;. Hepatocuprein. Oxidoreductase E.C.1.15.1.1 BRENDA | ||||||||||||
similarity | Belongs to the iron/manganese superoxide dismutase family.[Sod_Fe_C] | ||||||||||||||
subunit | Homotetramer. | ||||||||||||||
catalytic activ. | 2 superoxide + 2 h(+) = o(2) + h(2)o(2). | ||||||||||||||
subcellular loc. | Secreted protein. | ||||||||||||||
genes | sodB (A. fumigatus); SOD1 (B. taurus); sodA (D. radiodurans); sodA, sodB, sodC (E. coli); SOD1, SOD2 (H. sapiens); sod (M. thermoautotrophicum); MT0447, sodC (M. tuberculosis); sodC (P. leiognathi); sodB (P. gingivalis); sodA (P. freudenreichii); sodB (P. putida); sod (P. aerophilum); sodC1, sodC (S. typhimurium); SOD (S. mansoni); SODCP (S. oleracea); sodN (S. seoulensis); sod (S. acidocaldarius); sod (S. solfataricus); sodA (T. thermophilus); sod1-B (X. laevis); SOD1 (S. cerevisiae) | ||||||||||||||
function | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | ||||||||||||||
Gene Ontology |
| ||||||||||||||
disease | Amyotrophic lateral sclerosis,due to SOD1 deficiency Superoxide Dismutase 2; Sod2 | ||||||||||||||
Primary reference | X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions., Cooper JB, McIntyre K, Badasso MO, Wood SP, Zhang Y, Garbe TR, Young D, J Mol Biol 1995 Mar 3;246(4):531-44. PMID:7877174 |
Data retrieval |
View 1IDS in 3D |
|
Visual 3D analysis of 1IDS |
|
Structure-derived information |
- Domain d1idsa1, region A:2-85 [Jmol] [rasmolscript] [script source] - Domain d1idsa2, region A:86-199 [Jmol] [rasmolscript] [script source] - Domain d1idsb1, region B:2-85 [Jmol] [rasmolscript] [script source] - Domain d1idsb2, region B:86-199 [Jmol] [rasmolscript] [script source] - Domain d1idsc1, region C:2-85 [Jmol] [rasmolscript] [script source] - Domain d1idsc2, region C:86-199 [Jmol] [rasmolscript] [script source] - Domain d1idsd1, region D:2-85 [Jmol] [rasmolscript] [script source] - Domain d1idsd2, region D:86-199 [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
Other resources with information on 1IDS |
Movements, Movies and Images |